Disease relevance of LOC443489

• Phosphofructokinase (ATP : D-fructose-6-phosphate 1 phosphotransferase, EC 2.7.1.11) from two different lactobacilli, Lactobacillus plantarum and Lactobacillus acidophilus were isolated and purified [1].

High impact information on LOC443489

• Conditions for phosphofructokinase binding to myofibrils, as well as its dissociation, follow what was observed with the binding of phosphofructokinase to the particulate fraction [2].
• Amino acid sequence at the allosteric site of sheep heart phosphofructokinase [3].
• Heart phosphofructokinase. Allosteric kinetics following affinity labeling modification of the enzyme by 8-[m-(m-fluorosulfonylbenzamido) benzylthio] adenine [4].
• An adenine analog 8-[m-(m-fluorosulfonylbenzamido)benzylthio]adenine (FSB-adenine) reacts covalently with sheep heart phosphofructokinase [4].
• The allosteric regulation of heart phosphofructokinase was studied at pH 6.9 with an alternative substrate, fructose 6-sulfate [5].

Biological context of LOC443489

• The red cell total triose phosphate peaked and fell initially, followed by glucose-6-phosphate and 2,3-diphosphoglycerate suggesting inhibition of phosphofructokinase activity and a decrease in glycolysis secondary to decreased red cell intracellular pH [6].
• Phosphorylation of heart phosphofructokinase by Ca2+/calmodulin protein kinase [7].
• Antisera from sheep immunized against the purified phosphofructokinase from L. plantarum showed immunologic cross reaction with the enzyme from L. acidophilus [1].
• 2. Glucose infusion significantly increased the specific activities of phosphofructokinase, pyruvate kinase and 6-phosphogluconate dehydrogenase and significantly reduced the specific activity of glucose-6-phosphatase suggesting that the pathways of glucose breakdown are increased, and gluconeogenesis decreased, in glucose-infused animals [8].

Anatomical context of LOC443489

• However, if phosphofructokinase is assayed under these conditions while bound to myofibrils, the enzyme is activated [2].
• The change of 2,3-bisphosphoglycerate levels in rabbit but not in sheep erythrocytes could be explained by the changes of the phosphofructokinase/pyruvate kinase and 2,3-bisphosphoglycerate synthase/2,3-bisphosphoglycerate phosphatase activity ratios [9].
• In slow-twitch soleus muscle half-lives of phosphofructokinase, pyruvate kinase, hexokinase II and creatine kinase were 0.63 d, 0.72 d, 0.85 d and 0.82 d [10].

Associations of LOC443489 with chemical compounds

• Heart phosphofructokinase: allosteric kinetics with fructose 6-sulfate [5].
• Apparent half-lives of phosphofructokinase, pyruvate kinase and hexokinase I were 0.56 d, 0.73 d and 0.93 d in rabbit heart [10].
• Phosphorylation by either protein kinase caused a slight increase in the Km of PFK for fructose-6-P [7].
• Turnover rates of hexokinase I, phosphofructokinase, pyruvate kinase and creatine kinase in slow-twitch soleus muscle and heart of the rabbit [10].
• Affinity labeling of AMP-ADP sites in heart phosphofructokinase by 5-p-fluorosulfonylbenzoyl adenosine [11].

Other interactions of LOC443489

• Steady-state mRNA levels of alpha-enolase, lactate dehydrogenase A, and liver phosphofructokinase declined significantly postnatally [12].
• Aldolase A, beta-enolase, and muscle phosphofructokinase mRNA levels increased postnatally [12].
• As compared to the control muscles, stimulation led to significant increases in the amount of phosphofructokinase, aldolase and glyceraldehyde-3-phosphate dehydrogenase bound to the particulate fraction [13].
• Specific antisera against glycogen phosphorylase, phosphofructokinase, aldolase, glyceraldehyde-phosphate dehydrogenase, enolase, lactate dehydrogenase, cytosolic and mitochondrial malate dehydrogenase from rabbit muscle were obtained from sheep [14].

Analytical, diagnostic and therapeutic context of LOC443489

• HPLC analysis of phosphorylated PFK indicated that phosphorylation by CaM-kinase occurs at least at two sites that are distinct from those recognized by PKA [7].

References